ID A0A510DUY9_9CREN Unreviewed; 335 AA. AC A0A510DUY9; A0A510E2M3; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 02-DEC-2020, entry version 8. DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435}; DE Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435}; DE EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435}; DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435}; DE Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435}; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435}; GN Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435}; GN ORFNames=IC006_1298 {ECO:0000313|EMBL:BBG23997.1}, IC007_1273 GN {ECO:0000313|EMBL:BBG26752.1}; OS Sulfuracidifex tepidarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfuracidifex. OX NCBI_TaxID=1294262 {ECO:0000313|EMBL:BBG23997.1, ECO:0000313|Proteomes:UP000322983}; RN [1] {ECO:0000313|Proteomes:UP000322983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC-006 {ECO:0000313|Proteomes:UP000322983}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16833."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000325030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC-007 {ECO:0000313|Proteomes:UP000325030}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16834."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BBG23997.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IC-006 {ECO:0000313|EMBL:BBG23997.1}, and IC-007 RC {ECO:0000313|EMBL:BBG26752.1}; RA Itoh T., Miura T., Sakai H.D., Kato S., Ohkuma M., Takashina T.; RT "Sulfuracidifex tepidarius gen. nov., sp. nov. and transfer of Sulfolobus RT metallicus Huber and Stetter 1992 to the genus Sulfuracidifex as RT Sulfuracidifex metallicus comb. nov."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2020). CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids CC (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction CC of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In CC the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl CC migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the CC reductase reaction, this 2-ketoacid undergoes a metal-dependent CC reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. CC {ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2- CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00435}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2- CC ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00435}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|HAMAP-Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864, ECO:0000256|HAMAP- CC Rule:MF_00435}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|HAMAP-Rule:MF_00435, CC ECO:0000256|PROSITE-ProRule:PRU01198}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP018929; BBG23997.1; -; Genomic_DNA. DR EMBL; AP018930; BBG26752.1; -; Genomic_DNA. DR RefSeq; WP_054845646.1; NZ_BBCL01000003.1. DR GeneID; 41717616; -. DR KEGG; step:IC006_1298; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000322983; Chromosome. DR Proteomes; UP000325030; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013023; KARI. DR InterPro; IPR000506; KARI_C. DR InterPro; IPR013116; KARI_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. DR PROSITE; PS51851; KARI_C; 1. DR PROSITE; PS51850; KARI_N; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00435, ECO:0000256|PROSITE-ProRule:PRU01198}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304, KW ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-ProRule:PRU01198}; KW Isomerase {ECO:0000313|EMBL:BBG23997.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}; NADP {ECO:0000256|HAMAP-Rule:MF_00435}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE- KW ProRule:PRU01198}; Reference proteome {ECO:0000313|Proteomes:UP000322983}. FT DOMAIN 5..185 FT /note="KARI N-terminal Rossmann" FT /evidence="ECO:0000259|PROSITE:PS51850" FT DOMAIN 186..331 FT /note="KARI C-terminal knotted" FT /evidence="ECO:0000259|PROSITE:PS51851" FT NP_BIND 28..31 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT ACT_SITE 111 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT METAL 194 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 194 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 198 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 230 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT METAL 234 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" FT BINDING 56 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 137 FT /note="NADP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435" FT BINDING 255 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00435, FT ECO:0000256|PROSITE-ProRule:PRU01198" SQ SEQUENCE 335 AA; 36889 MW; E5EDD717F07E845D CRC64; MINIAKIYTD KDASLDALKG KKIAVLGYGN QGRAWALNLR DSGLDVTVGL ERQGKSWEKA TKDGFTPVKT DEAVRNAEVI IFLVPDMIQR TIWLEKVKPN MKKGADLVFA HGFNIHFRMI EPPADSDVYM VAPKGPGDTV RDYYVAGGGV PVLVAAYQNV SGKAMEKALA VAKGIGATRS GALESSFKEE TETDLVGEQT ILVGGIMELM RASFETLVEM GYQPEVAYFE TINEVKMIVD IIHSKGLSGM LRAVSDTAKY GGMTVGKKVI NEDVRKRIRE AAERVRDGQF ASEWVEEYNR GMPTVVNGLK EVDNSLEQKV ANELRDLIER GKPKK //